The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities
In many animals, the germ plasm segregates germline from soma during early development. Oskar protein is known for its ability to induce germ plasm formation and germ cells in Drosophila. However, the molecular basis of germ plasm formation remains unclear. Here, we show that Oskar is an RNA-binding...
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Elsevier
2015-07-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124715006816 |
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doaj-49796906f431473ea5e6f5b5580368ae2020-11-25T01:51:02ZengElsevierCell Reports2211-12472015-07-0112458759810.1016/j.celrep.2015.06.055The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding ActivitiesMandy Jeske0Matteo Bordi1Sebastian Glatt2Sandra Müller3Vladimir Rybin4Christoph W. Müller5Anne Ephrussi6Developmental Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyDevelopmental Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyDevelopmental Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyProtein Expression and Purification Core Facility, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyStructural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyDevelopmental Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, GermanyIn many animals, the germ plasm segregates germline from soma during early development. Oskar protein is known for its ability to induce germ plasm formation and germ cells in Drosophila. However, the molecular basis of germ plasm formation remains unclear. Here, we show that Oskar is an RNA-binding protein in vivo, crosslinking to nanos, polar granule component, and germ cell-less mRNAs, each of which has a role in germline formation. Furthermore, we present high-resolution crystal structures of the two Oskar domains. RNA-binding maps in vitro to the C-terminal domain, which shows structural similarity to SGNH hydrolases. The highly conserved N-terminal LOTUS domain forms dimers and mediates Oskar interaction with the germline-specific RNA helicase Vasa in vitro. Our findings suggest a dual function of Oskar in RNA and Vasa binding, providing molecular clues to its germ plasm function.http://www.sciencedirect.com/science/article/pii/S2211124715006816 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Mandy Jeske Matteo Bordi Sebastian Glatt Sandra Müller Vladimir Rybin Christoph W. Müller Anne Ephrussi |
| spellingShingle |
Mandy Jeske Matteo Bordi Sebastian Glatt Sandra Müller Vladimir Rybin Christoph W. Müller Anne Ephrussi The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities Cell Reports |
| author_facet |
Mandy Jeske Matteo Bordi Sebastian Glatt Sandra Müller Vladimir Rybin Christoph W. Müller Anne Ephrussi |
| author_sort |
Mandy Jeske |
| title |
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities |
| title_short |
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities |
| title_full |
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities |
| title_fullStr |
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities |
| title_full_unstemmed |
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities |
| title_sort |
crystal structure of the drosophila germline inducer oskar identifies two domains with distinct vasa helicase- and rna-binding activities |
| publisher |
Elsevier |
| series |
Cell Reports |
| issn |
2211-1247 |
| publishDate |
2015-07-01 |
| description |
In many animals, the germ plasm segregates germline from soma during early development. Oskar protein is known for its ability to induce germ plasm formation and germ cells in Drosophila. However, the molecular basis of germ plasm formation remains unclear. Here, we show that Oskar is an RNA-binding protein in vivo, crosslinking to nanos, polar granule component, and germ cell-less mRNAs, each of which has a role in germline formation. Furthermore, we present high-resolution crystal structures of the two Oskar domains. RNA-binding maps in vitro to the C-terminal domain, which shows structural similarity to SGNH hydrolases. The highly conserved N-terminal LOTUS domain forms dimers and mediates Oskar interaction with the germline-specific RNA helicase Vasa in vitro. Our findings suggest a dual function of Oskar in RNA and Vasa binding, providing molecular clues to its germ plasm function. |
| url |
http://www.sciencedirect.com/science/article/pii/S2211124715006816 |
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